1MM8

Crystal structure of Tn5 Transposase complexed with ME DNA

1MM8 の概要

• エントリーDOI: 10.2210/pdb1mm8/pdb
• 関連するPDBエントリー: 1F3I 1L1A
• 分子名称: ME DNA transferred strand, ME DNA non-transferred strand, Tn5 Transposase, ... (5 entities in total)
• 機能のキーワード: protein-dna complex, transcription-dna complex, transcription/dna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 66221.58

構造登録者

Steiniger-White, M.,Bhasin, A.,Lovell, S.,Rayment, I.,Reznikoff, W.S. (登録日: 2002-09-03, 公開日: 2002-12-13, 最終更新日: 2024-02-14)

主引用文献

Steiniger-White, M.,Bhasin, A.,Lovell, S.,Rayment, I.,Reznikoff, W.S.
Evidence for "unseen" Transposase--DNA contacts
J.Mol.Biol., 322:971-982, 2002

PubMed Abstract: In this study, evidence of novel, important interactions between a hyperactive Tn5 transposon recognition end sequence and hyperactive Tn5 transposase (Tnp) are presented. A hyperactive Tn5 end sequence, the mosaic end (ME), was isolated previously. The ME and a wild-type end sequence, the outside end (OE), differ at only three positions, yet transposition on the ME is tenfold higher than on the OE in vivo. Also, transposition on the ME is much more efficient than transposition on the OE in vitro. Here, we show that the decreased activity observed for the OE is caused by a defect in paired ends complex (PEC) formation resulting from the orientation of the A-T base-pair at position 4 of this end. Efficient PEC formation requires an interaction between the C5-methyl group (C5-Me) on the non-transferred strand thymine base at position 4 (T4) and Tnp. PEC formation on nicked substrates is much less affected by the orientation of the A-T base-pair at position 4, indicating that the C5-Me group is important only for steps preceding nicking. A recently determined co-crystal structure of Tn5 Tnp with the ME is discussed and a model explaining possible roles for the base-pair at position 4 is explored.

PubMed: 12367522
DOI: 10.1016/S0022-2836(02)00877-X

実験手法

X-RAY DIFFRACTION (2.8 Å)